A new l -glutaminase from Kosakonia sp.: extracellular production, gene identification and structural analysis
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ORIGINAL PAPER
A new l‑glutaminase from Kosakonia sp.: extracellular production, gene identification and structural analysis Aizi Nor Mazila Ramli1,2 · Nur Dini Johari1 · Mohd Akmal Azhar3 · Rohaida Che Man3 · Hazrulrizawati Abd Hamid1 Received: 30 January 2020 / Accepted: 28 September 2020 © Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract A comprehensive research has been carried out on l-glutaminase producers from marine bacteria. Among the evaluated isolates, Kosakonia radicincitans was found to be a l-glutaminase producer from a marine environment, having the highest enzymatic activities. The optimal condition for l-glutaminase production from K. radicincitans was at pH and temperature of 7.0 and 37 °C, respectively. The enzyme was found stable between pH 4 and 8 and its function also maintained at temperatures between 31 and 43 °C after 30-min incubation. Both the amino acid sequence and domain analysis of the l-glutaminase from the Kosakonia strains revealed various similarities and dissimilarities between these amidase enzymes. Sequence analysis and comparison of l-glutaminase from Kosakonia sp. with other l-glutaminase along with structural prediction were able to identify the unique characteristics of the predicted structures and offer a different perspective into their distinguishable properties for industrial use. Keywords l-glutaminase · Kosakonia radicincitans · 3D model
Introduction l -glutaminase
(l-glutamine amidohydrolase EC 3.5.1.2) is the enzyme responsible in catalyzing the hydrolysis of l-glutamine to l-glutamic acid and ammonia [18]. Over the years, l-glutaminase is getting popular and has attracted considerable attention in both food and pharmaceutical industrial applications. In the food industry, l-glutaminase takes a major part that controls the delicious taste of fermented condiments; such as soy sauce and in general, food products; by increasing the glutamic acid content, which is a widely acclaimed flavor-enhancing amino acid [42]. In spite of its demonstrated potential as a flavor-enhancing
* Aizi Nor Mazila Ramli [email protected] 1
College of Computing and Applied Sciences, Faculty of Industrial Sciences and Technology, Universiti Malaysia Pahang, Lebuhraya Tun Razak, Gambang, 26300 Kuantan, Pahang, Malaysia
2
Bio Aromatic Research Centre of Excellence, Universiti Malaysia Pahang, Lebuhraya Tun Razak, Gambang, 26300 Kuantan, Pahang Darul Makmur, Malaysia
3
Department of Chemical Engineering, College of Engineering, Universiti Malaysia Pahang, Lebuhraya Tun Razak, 26300 Gambang, Pahang, Malaysia
agent, this enzyme is proposed as an important therapeutic agent for cancer therapy, especially for acute lymphocytic leukemia, in combination or as an alternative, to l-asparaginase. The action of l-glutaminase as an anti-carcinogenic associate with the inability of the lymphatic tumor cell to synthesize glutamine has caused glutamine depletion [1]. l-glutaminase can be derived from plant and animal tissues. However, microorganisms, such as
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